PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27250206-0 2016 Structure of Complement C3(H2O) Revealed By Quantitative Cross-Linking/Mass Spectrometry And Modeling. Water 27-30 complement C3 Homo sapiens 13-26 28192370-10 2017 The loaded C3(H2O) represents a source of C3a, and its uptake altered the cytokine profile of activated CD4+ T cells. Water 14-17 complement C3 Homo sapiens 42-45 27976756-2 2016 We have used QCLMS to understand the final maturation step of the proteasome lid and also to elucidate the structure of complement C3(H2O). Water 134-137 complement C3 Homo sapiens 120-133 30300780-4 2018 With the application of excitation emission matrix-parallel factor analysis (EEM-PARAFAC), we found that I-THM formation in UV-chloraminated water correlated well with two ratios of three PARAFAC humic-like components (C3/C2 and C1/C2, R2 = 0.958-1.000), suggesting that the ratios of fluorescent components can be used as reliable indicators for I-THM formation. Water 141-146 complement C3 Homo sapiens 219-234 28169026-5 2017 Among the five fluorescent components, those associated to humic-like matter (C1, C3 and C4) showed a similar season variability in the river water feeding the DWTP (which resembled that of UV254 and TOC), whereas the two components associated to protein-like matter (C2 and C5) exhibited a different behavior. Water 142-147 complement C3 Homo sapiens 39-91 27250206-4 2016 This revealed details of the structural differences and similarities between C3(H2O) and C3, as well as between C3(H2O) and its pivotal proteolytic cleavage product, C3b, which shares functionally similarity with C3(H2O). Water 115-118 complement C3 Homo sapiens 166-169 27250206-5 2016 Considered in combination with the crystal structures of C3 and C3b, the QCMLS data suggest that C3(H2O) generation is accompanied by the migration of the thioester-containing domain of C3 from one end of the molecule to the other. Water 100-103 complement C3 Homo sapiens 64-67 27250206-8 2016 The unique arrangement of domains thus observed in C3(H2O), which retains the anaphylatoxin domain (that is excised when C3 is enzymatically activated to C3b), can be used to rationalize observed differences between C3(H2O) and C3b in terms of complement activation and regulation. Water 54-57 complement C3 Homo sapiens 154-157 27250206-8 2016 The unique arrangement of domains thus observed in C3(H2O), which retains the anaphylatoxin domain (that is excised when C3 is enzymatically activated to C3b), can be used to rationalize observed differences between C3(H2O) and C3b in terms of complement activation and regulation. Water 54-57 complement C3 Homo sapiens 228-231 27250206-8 2016 The unique arrangement of domains thus observed in C3(H2O), which retains the anaphylatoxin domain (that is excised when C3 is enzymatically activated to C3b), can be used to rationalize observed differences between C3(H2O) and C3b in terms of complement activation and regulation. Water 219-222 complement C3 Homo sapiens 154-157 27250206-8 2016 The unique arrangement of domains thus observed in C3(H2O), which retains the anaphylatoxin domain (that is excised when C3 is enzymatically activated to C3b), can be used to rationalize observed differences between C3(H2O) and C3b in terms of complement activation and regulation. Water 219-222 complement C3 Homo sapiens 228-231 24764271-4 2015 beta-Dicalcium silicate (beta-C2S) and tricalcium aluminate (C3A) are Portland cement components, these compounds react with water to form hydrated phases that enhance mechanical strength of the end products. Water 125-130 complement C3 Homo sapiens 61-64 12892940-1 2003 A butenolide-containing sugar available from the aldol condensation of methyl 4,6-O-benzylidene-alpha-D-glucopyranosid-2-ulose with diethyl malonate is autoxidized at the C-3 position into the corresponding alpha,beta-unsaturated gamma-lactone sugar by air, which subsequently undergoes 1,4-conjugate (Michael) addition of hydroxide ion (or water) leading to a C-branched-chain glucopyranosidulose. Water 341-346 complement C3 Homo sapiens 171-174 23677468-7 2013 Activation of the alternative pathway on activated platelets occurs when properdin is on the surface and recruits C3b or C3(H2O) to form C3b,Bb or a novel cell-bound C3 convertase [C3(H2O),Bb], which normally is present only in the fluid phase. Water 124-127 complement C3 Homo sapiens 137-140 20002318-1 2010 Experimental evidence demonstrates a higher efficiency of water and nitrogen use in C(4) compared with C(3) plants, which is hypothesized to drive differences in biomass allocation between C(3) and C(4) species. Water 58-63 complement C3 Homo sapiens 189-193 17479294-7 2007 However, during dry periods, most C(3) species used proportionally more water from deeper portions of the soil profile relative to the C(4) grasses. Water 72-77 complement C3 Homo sapiens 34-38 20428523-0 2010 Ruthenium/TFA-catalyzed regioselective C-3-alkylation of indoles with terminal alkynes in water: efficient and unprecedented access to 3-(1-methylalkyl)-1H-indoles. Water 90-95 complement C3 Homo sapiens 39-42 19891460-5 2009 The other involves a transient oxocarbenium zwitterionic intermediate, formed by direct attack of C3(PEP) onto C1(A5P), followed by reaction of water at C2. Water 144-149 complement C3 Homo sapiens 98-117 15110934-2 2004 Using the synchrotron small-angle X-ray diffraction (SAXD), it is shown that the C3A anesthetic induces the cubic and hexagonal (H(I)) phases at 2 > or = C3A:EYPC > 0.5 and H2O:EYPC < or = 40 molar ratios. Water 179-182 complement C3 Homo sapiens 81-84 15065850-1 2004 trans-3-Chloroacrylic acid dehalogenase (CaaD) converts trans-3-chloroacrylic acid to malonate semialdehyde by the addition of H(2)O to the C-2, C-3 double bond, followed by the loss of HCl from the C-3 position. Water 127-132 complement C3 Homo sapiens 145-148 15065850-1 2004 trans-3-Chloroacrylic acid dehalogenase (CaaD) converts trans-3-chloroacrylic acid to malonate semialdehyde by the addition of H(2)O to the C-2, C-3 double bond, followed by the loss of HCl from the C-3 position. Water 127-132 complement C3 Homo sapiens 199-202 12036059-6 2002 The results showed that dehydrogenation occurred randomly at the positions where hydroxyl groups are attached, but the most preferred position was C-3 and the radical position moved from C-3 to C-4 by the elimination of water molecule. Water 220-225 complement C3 Homo sapiens 147-150 12036059-6 2002 The results showed that dehydrogenation occurred randomly at the positions where hydroxyl groups are attached, but the most preferred position was C-3 and the radical position moved from C-3 to C-4 by the elimination of water molecule. Water 220-225 complement C3 Homo sapiens 187-190 7850393-0 1994 Mutagenic and carcinogenic risk of oxygen containing chlorinated C-3 hydrocarbons: putative secondary products of C-3 chlorohydrocarbons and chlorination of water. Water 157-162 complement C3 Homo sapiens 65-68 10587314-7 1999 cyclo(-D-Asp1-Asp2-Gly3-Ahd4-Ahd5-Gly6-) (C3) clearly exhibits two different conformations with a shifted beta,beta-turn motif in CDCI3 and SDS/H2O solutions. Water 144-147 complement C3 Homo sapiens 42-44 7850393-1 1994 Oxygen containing C-3 chlorohydrocarbons are secondary products of C-3 chlorohydrocarbons formed during oxidation at air, in the metabolism of pesticides and by chlorination of drinking water. Water 186-191 complement C3 Homo sapiens 18-21 7850393-1 1994 Oxygen containing C-3 chlorohydrocarbons are secondary products of C-3 chlorohydrocarbons formed during oxidation at air, in the metabolism of pesticides and by chlorination of drinking water. Water 186-191 complement C3 Homo sapiens 67-70 2760472-4 1989 C3(H2O) eluted as a homogeneous peak well resolved from native C3, C3b, high molecular weight aggregates and small degradation fragments. Water 3-6 complement C3 Homo sapiens 67-70 1939111-6 1991 The hydrogen atom at C-3 of the enzyme product is introduced from solvent water. Water 74-79 complement C3 Homo sapiens 21-24 2311295-7 1990 A second rise of C3a levels and C3a:C3 ratio from day 4 on paralleled the course of extravascular lung water. Water 103-108 complement C3 Homo sapiens 17-20 2311295-7 1990 A second rise of C3a levels and C3a:C3 ratio from day 4 on paralleled the course of extravascular lung water. Water 103-108 complement C3 Homo sapiens 32-35 35134220-2 2022 Here, we aimed to clarify how stomatal dynamics and water use efficiency (WUE) differ in fluctuating environments in major C3 and C4 crops. Water 52-57 complement C3 Homo sapiens 123-132 35329749-0 2022 Effect of Water-Solid Mixing Sequence and Crystallization Water of Calcium Sulphate on the Hydration of C3A. Water 10-15 complement C3 Homo sapiens 104-107 35329749-0 2022 Effect of Water-Solid Mixing Sequence and Crystallization Water of Calcium Sulphate on the Hydration of C3A. Water 58-63 complement C3 Homo sapiens 104-107 8417970-3 1993 The rise of rotator content at a urea concentration C3 > or = C3* when the bulk water is practically exhausted is suggested as a main driving force of protein unfolding. Water 83-88 complement C3 Homo sapiens 65-68 35329749-6 2022 Effects of calcium sulphate with different amounts of crystallisation water (anhydrite, hemihydrate and gypsum) on C3A hydration are also investigated, and it is found that the water of crystallisation does not have a significant impact on the kinetics of reaction or the formed hydrate phase assemblage. Water 177-182 complement C3 Homo sapiens 115-118 2457622-2 1988 Hydrolysis of the internal thioester bond in native C3 is thought to be a key event in initiating the alternative pathway of C activation, because the resulting C3(H2O) acquires "C3b-like" properties. Water 164-167 complement C3 Homo sapiens 179-182 6610676-5 1984 The circular dichroism spectra of synthetic peptides corresponding to sequences 57-77, 65-77, and 73-77 in human C3a were measured in water and trifluoroethanol. Water 134-139 complement C3 Homo sapiens 113-116 6586103-4 1983 The product, C3(H2O), is functionally C3b-like and forms a C3 convertase with Factors B and D. The resulting biomolecular enzyme, C3(H2O),Bb, is a serine protease that cleaves C3 generating metastable C3b. Water 16-19 complement C3 Homo sapiens 38-41 6586103-4 1983 The product, C3(H2O), is functionally C3b-like and forms a C3 convertase with Factors B and D. The resulting biomolecular enzyme, C3(H2O),Bb, is a serine protease that cleaves C3 generating metastable C3b. Water 16-19 complement C3 Homo sapiens 201-204 6586103-4 1983 The product, C3(H2O), is functionally C3b-like and forms a C3 convertase with Factors B and D. The resulting biomolecular enzyme, C3(H2O),Bb, is a serine protease that cleaves C3 generating metastable C3b. Water 133-136 complement C3 Homo sapiens 38-41 6586103-4 1983 The product, C3(H2O), is functionally C3b-like and forms a C3 convertase with Factors B and D. The resulting biomolecular enzyme, C3(H2O),Bb, is a serine protease that cleaves C3 generating metastable C3b. Water 133-136 complement C3 Homo sapiens 201-204 6586103-6 1983 C3(H2O),Bb produces only three to five metastable C3b molecules per enzyme before being inactivated by regulatory proteins. Water 3-6 complement C3 Homo sapiens 50-53 1156576-11 1975 Exhaustive incubation of the tritiated malate (3-H/14-C = 1.95) with fumarase to labilize the pro-R hydrogen at C-3 resulted in release of 65% of the tritium into water. Water 163-168 complement C3 Homo sapiens 112-115 6903192-10 1980 These results suggest that the initial C3 convertase of the alternative pathway may be formed from native C3, without proteolysis, by the attack of a variety of nucleophiles including water. Water 184-189 complement C3 Homo sapiens 39-41 6903192-10 1980 These results suggest that the initial C3 convertase of the alternative pathway may be formed from native C3, without proteolysis, by the attack of a variety of nucleophiles including water. Water 184-189 complement C3 Homo sapiens 106-108 6903192-14 1980 These findings are consistent with the concept that native C3 contains an active carbonyl group, probably in the form of a thioester, which can either react with water to form functionally C3b-l;ike C3 or, upon enzymatic conversion of C3 to C3b, allows C3b to form an ester bond with hydroxyl groups on the target surface. Water 162-167 complement C3 Homo sapiens 59-61 6903192-14 1980 These findings are consistent with the concept that native C3 contains an active carbonyl group, probably in the form of a thioester, which can either react with water to form functionally C3b-l;ike C3 or, upon enzymatic conversion of C3 to C3b, allows C3b to form an ester bond with hydroxyl groups on the target surface. Water 162-167 complement C3 Homo sapiens 189-192 32296436-3 2020 This results in the formation of non-proteolytically activated C3(H2O) which is believed have C3b-like properties and be able to form an active initial fluid phase C3 convertase together with Factor B (FB). Water 66-69 complement C3 Homo sapiens 94-97 33549622-9 2021 This work showed that Mg-rich C3A is a promising candidate for simultaneous removal of NH4+ and PO43-, shedding light on practical water remediation. Water 131-136 complement C3 Homo sapiens 30-33 33513980-10 2021 This model can reflect the hydration characteristics of C3A in different stages, and quantify the response of the hydration process of C3A to different gypsum content, water-cement ratio, and particle size distribution. Water 168-173 complement C3 Homo sapiens 135-138 31446306-2 2019 Generation of the "C3b-like" C3(H2O) has been described as essential for AP activation, since it conveniently explains how the initial fluid-phase AP convertase of the amplification loop is generated. Water 32-35 complement C3 Homo sapiens 19-22 31336566-8 2019 CaO grains were bonded by the formed tricalcium aluminate (C3A) and the apparent porosity of the sample was reduced, reducing the contact area of CaO with water vapor. Water 155-160 complement C3 Homo sapiens 59-62 30763638-1 2019 A Mg2+-water bridge between the C-3, C-4 diketo moiety of fluoroquinolones and the conserved amino acid residues in the GyrA/ParC subunit is critical for the binding of a fluoroquinolone to a topoisomerase-DNA covalent complex. Water 7-12 complement C3 Homo sapiens 32-35